Continued from EC 3.6.1 and EC 3.6.2
EC 3.6.3 Acting on acid anhydrides; catalysing transmembrane movement of substances
Accepted name: phospholipid-translocating ATPase
Reaction: ATP + H2O + phospholipid[side 1] = ADP + phosphate + phospholipid[side 2]
Other name(s): Mg2+-ATPase; flippase; aminophospholipid-transporting ATPase
Systematic name: ATP phosphohydrolase (phospholipid-flipping)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other ('flippase').
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823-832. [PMID: 8136700]
2. Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95-102. [PMID: 8839453]
3. Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429-10434. [PMID: 9099684]
4. Auland ME, Roufogalis BD, Devaux PF, Zachowski A. Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes. Proc Natl Acad Sci USA 91 (1994) 10938-10942. [PMID: 7971987]
Accepted name: Mg2+-importing ATPase
Reaction: ATP + H2O + Mg2+out = ADP + phosphate + Mg2+in
Systematic name: ATP phosphohydrolase (Mg2+-importing)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in both Gram-positive and Gram-negative bacteria, and three types are known, designated as CorA, MgtA and MgtB. The CorA itself is not an ATPase but an Mg2+ transporter.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Tao, T., Snavely, M.D., Farr, S.G. and Maguire, M.E. Magnesium transport in Salmonella typhimurium: mtgA encodes a P-type ATPase and is regulated by Mg2+ in a manner similar to that of the mgtB P-type ATPase. J. Bacteriol. 177 (1995) 2654-2662. [PMID: 7751273]
2. Smith, R.L., Szegedy, M.A., Kucharski, L.M., Walker, C., Wiet, R.M., Redpath, A., Kaczmarek, M.T. and Maguire, M.E. The CorA Mg2+ transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the third membrane domain identifies a Mg2+ pore. J. Biol. Chem. 273 (1998) 28663-28669. [PMID: 9786860]
Accepted name: Cd2+-exporting ATPase
Reaction: ATP + H2O + Cd2+in = ADP + phosphate + Cd2+out
Systematic name: ATP phosphohydrolase (Cd2+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Silver, S. and Ji, G. Newer systems for bacterial resistance to toxic heavy metals. Environ. Health Perspect. 102, Suppl. 3 (1994) 107-113. [PMID: 7843081]
2. Tsai, K.J. and Linet, A.L. Formation of a phosphorylated enzyme intermediate by the cadA Cd2+-ATPase. Arch. Biochem. Biophys. 305 (1993) 267-270. [PMID: 8373163]
Accepted name: Cu2+-exporting ATPase
Reaction: ATP + H2O + Cu2+in = ADP + phosphate + Cu2+out
Systematic name: ATP phosphohydrolase (Cu2+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This bacterial and mammalian enzyme exports Cu2+ from cells. In humans, it is involved in Menkes disease and Wilson's disease.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Vulpe, C., Levinson, B., Whitney, S., Packman, S. and Gitschier, J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat. Genet. 3 (1993) 7-13. [PMID: 8490659]
2. Petrukhin, K., Lutsenko, S., Chernov, I., Ross, B.M., Kaplan, J.H. and Gilliam, T.C. Characterization of the Wilson disease gene encoding a P-type copper-transporting ATPase: genomic organization, alternative splicing, and structure/function predictions. Hum. Mol. Genet. 3 (1994) 1647-1656. [PMID: 7833924]
3. Fagan, M.J. and Saier, M.H., Jr. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 38 (1994) 57-99. [PMID: 8151716]
Accepted name: Zn2+-exporting ATPase
Reaction: ATP + H2O + Zn2+in = ADP + phosphate + Zn2+out
Other name(s): Zn(II)-translocating P-type ATPase; P1B-type ATPase; AtHMA4
Systematic name: ATP phosphohydrolase (Zn2+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme also exports Cd2+ and Pb2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Beard, S.J., Hashim, R., Membrillo-Hernández, J., Hughes, M.N. and Poole, R.K. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase. Mol. Microbiol. 25 (1997) 883-891. [PMID: 9364914]
2. Rensing, C., Mitra, B. and Rosen, B.P. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc. Natl. Acad. Sci. USA 94 (1997) 14326-14331. [PMID: 9405611]
3. Rensing, C., Sun, Y., Mitra, B. and Rosen, B.P. Pb(II)-translocating P-type ATPases. J. Biol. Chem. 273 (1998) 32614-32617. [PMID: 9830000]
4. Mills, R.F., Francini, A., Ferreira da Rocha, P.S., Baccarini, P.J., Aylett, M., Krijger, G.C. and Williams, L.E. The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels. FEBS Lett. 579 (2005) 783-791. [PMID: 15670847]
5. Eren, E. and Arguello, J.M. Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasis. Plant Physiol. 136 (2004) 3712-3723. [PMID: 15475410]
Accepted name: H+-exporting ATPase
Reaction: ATP + H2O + H+in = ADP + phosphate + H+out
Other name(s): proton-translocating ATPase; yeast plasma membrane H+-ATPase; yeast plasma membrane ATPase; ATP phosphohydrolase
Systematic name: ATP phosphohydrolase (H+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Goffeau, A. and Slayman, C. The proton-translocating ATPase of the fungal plasma membrane. Biochim. Biophys. Acta 639 (1981) 197-223. [PMID: 6461354]
2. Serrano, R., Kielland-Brandt, M.C. and Fink, G.R. Yeast plasma membrane ATPase is essential for growth and has homology with (Na++K+)-, K+-and Ca2+-ATPases. Nature 319 (1986) 689-693. [PMID: 3005867]
3. Serrano, R. and Portillo, F. Catalytic and regulatory sites of yeast plasma membrane H+-ATPase studied by directed mutagenesis. Biochim. Biophys. Acta 1018 (1990) 195-199. [PMID: 2144186]
Accepted name: Na+-exporting ATPase
Reaction: ATP + H2O + Na+in = ADP + phosphate + Na+out
Systematic name: ATP phosphohydrolase (Na+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wieland, J., Nitsche, A.M., Strayle, J., Steiner, H. and Rudolph, H.K. The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane. EMBO J. 14 (1995) 3870-3882. [PMID: 7664728]
2. Catty, P., de Kerchove d'Exaerde, A. and Goffeau, A. The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett. 409 (1997) 325-332. [PMID: 9224683]
3. Cheng, J., Guffanti, A.A. and Krulwich, T.A. A two-gene ABC-type transport system that extrudes Na+ in Bacillus subtilis is induced by ethanol or protonophore. Mol. Microbiol. 23 (1997) 1107-1120. [PMID: 9106203]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: Ca2+-transporting ATPase
Reaction: ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
Other name(s): sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca2+-ATPase; calcium pump; Ca2+-pumping ATPase; plasma membrane Ca-ATPase
Systematic name: ATP phosphohydrolase (Ca2+-transporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in yeast. The first and third transport one ion per ATP hydrolysed, whereas the second transports two ions. Ca2+ is transported from the cytosol [side 1] into the sarcoplasmic reticulum in muscle cells [side 2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Schatzmann, H.J. and Vicenzi, F.F. Calcium movements across the membrane of human red cells. J. Physiol. 201 (1969) 369-395. [PMID: 4238381]
2. Inesi, G., Watanabe, T., Coan, C. and Murphy, A. The mechanism of sarcoplasmic reticulum ATPase. Ann. N.Y. Acad. Sci. 402 (1982) 515-532. [PMID: 6301340]
3. Carafoli, E. The Ca2+ pump of the plasma membrane. J. Biol. Chem. 267 (1992) 2115-2118. [PMID: 1310307]
4. MacLennan, D.H., Rice, W.J. and Green, N.M. The mechanism of Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases. J. Biol. Chem. 272 (1997) 28815-28818. [PMID: 9360942]
5. Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647-655. [PMID: 10864315]
Accepted name: Na+/K+-exchanging ATPase
Reaction: ATP + H2O + Na+in + K+out = ADP + phosphate + Na+out + K+in
Systematic name: ATP phosphohydrolase (Na+/K+-exchanging)
Other name: sodium pump; Na+,K+ pump; Na,K-pump; (Na+ + K+)-activated ATPase; (Na+ + K+)-ATPase; Na+,K+-ATPase; Na,K-activated ATPase
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na+ and influx of two K+ per ATP hydrolysed. It is involved in generating the plasma membrane electrical potential.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Skou, J.C. The influence of some cations on an adenosinetriphosphatase from peripheral nerve. Biochim. Biophys. Acta 23 (1957) 394-401.
2. Post, R.L., Sen, A.K. and Rosenthal, A.S. A phosphorylated intermediate in adenosine triphosphate-dependent sodium and potassium transport across kidney membrane. J. Biol. Chem. 240 (1965) 1437-1445.
3. Skou, J.C. The energy-coupled exchange of Na+ for K+ across the cell membrane. The Na+,K+ pump. FEBS Lett. 268 (1990) 314-324. [PMID: 2166689]
Accepted name: H+/K+-exchanging ATPase
Reaction: ATP + H2O + H+in + K+out = ADP + phosphate + H+out + K+in
Other name(s): H+-K+-ATPase; H,K-ATPase; (K+ + H+)-ATPase
Systematic name: ATP phosphohydrolase (H+/K+-exchanging)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A gastric mucosal enzyme that catalyses the efflux of one H+ and the influx of one K+ per ATP hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Sachs, G., Collier, R.H., Shoemaker, R.L. and Hirschowitz, B.I. The energy source for gastric H+ secretion. Biochim. Biophys. Acta 162 (1968) 210-219. [PMID: 5682852]
2. Hersey, S.J., Perez, A. Matheravidathu, S. and Sachs, G. Gastric H+-K+-ATPase in situ: evidence for compartmentalization. Am. J. Physiol. 257 (1989) G539-G547. [PMID: 2552824]
3. Rabon, E.C. and Reuben, M.A. The mechanism and structure of the gastric H,K-ATPase. Annu. Rev. Physiol. 52 (1990) 321-344. [PMID: 2158765]
Accepted name: Cl--transporting ATPase
Reaction: ATP + H2O + Cl-out = ADP + phosphate + Cl-in
Other name(s): Cl--translocating ATPase; Cl--motive ATPase
Systematic name: ATP phosphohydrolase (Cl--importing)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. An animal and plant enzyme involved in the import of chloride anions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ohhashi, T., Katsu, T. and Ikeda, M. Improvement of reconstitution of the Cl--translocating ATPase isolated from Acetabularia acetabulum into liposomes and several anion pump characteristics. Biochim. Biophys. Acta 1106 (1992) 165-170. [PMID: 1533790]
2. Gerencser, G.A. and Purushotham, K.R. Reconstituted Cl- pump protein: a novel Cl--motive ATPase. J. Bioenerget. Biomembr. 28 (1996) 459-469. [PMID: 8953378]
3. Inagaki, C., Hara, M. and Zeng, X.T. A Cl- pump in rat brain neurons. J. Exp. Zool. 275 (1996) 262-268. [PMID: 8759922]
Accepted name: K+-transporting ATPase
Reaction: ATP + H2O + K+out = ADP + phosphate + K+in
Other name(s): K+-translocating Kdp-ATPase; multi-subunit K+-transport ATPase
Systematic name: ATP phosphohydrolase (K+-importing)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme of di(heterotetrameric) structure that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Siebers, A. and Altendorf, K. Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli. J. Biol. Chem 264 (1989) 5831-5838. [PMID: 2522440]
2. Gassel, M., Siebers, A., Epstein, W. and Altendorf, K. Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli. Biochim. Biophys. Acta 1415 (1998) 77-84. [PMID: 9858692]
[EC 3.6.3.13 Deleted entry: identical to EC 3.6.3.1 (EC 3.6.3.13 created 2000, deleted 2001)]
Accepted name: H+-transporting two-sector ATPase
Reaction: ATP + H2O + H+in = ADP + phosphate + H+out
Glossary: Fo the "o" refers to oligomycin. F0 is incorrect.
Other names: ATP synthase; F1-ATPase; FoF1-ATPase; H+-transporting ATPase; mitochondrial ATPase; coupling factors (F0, F1 and CF1); chloroplast ATPase; bacterial Ca2+/Mg2+ ATPase
Systematic name: ATP phosphohydrolase (H+-transporting)
Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 α- and 3 β-subunits) is connected via the δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9-12 c subunits rotate by consecutive 120° angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archebacterial) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Boyer, P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215-250. [PMID: 8417777]
2. Abrahams, J.P., Leslie, A.G.W., Lutter, R. and Walker, J.F. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 375 (1994) 621-628. [PMID: 8065448]
3. Blair, A., Ngo, L., Park, J., Paulsen, I.T. and Saier, M.H., Jr. Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the FoF1-ATPases of bacteria, chloroplasts and mitochondria. Microbiology 142 (1996) 17-32. [PMID: 8581162]
4. Noji, H., Yasuda, R., Yoshida, M. and Kinosita, K., Jr. Direct observation of the rotation of F1-ATPase. Nature 386 (1997) 299-302. [PMID: 9069291]
Accepted name: Na+-transporting two-sector ATPase
Reaction: ATP + H2O + Na+in = ADP + phosphate + Na+out
Systematic name: ATP phosphohydrolase (Na+-transporting)
Other name: ATP synthase; vacuolar-type Na+-ATPase; Na+-translocating ATPase; Na+-translocating F1Fo-ATPase; vacuolar-type Na+-translocating ATPase
Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. An enzyme found in alkaliphilic bacteria that is similar to EC 3.6.3.14 (H+-transporting two-sector ATPase) where Na+ replaces H+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Solioz, M. and Davies, K. Operon of vacuolar-type Na+-ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 9453-9459. [PMID: 8144530]
2. Takase, K., Kakinuma, S., Yamato, I., Konishi, K., Igarashi, K. and Kanikuma, Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 11037-11044. [PMID: 8157629]
3. Rahlfs, S. and Müller, V. Sequence of subunit c of the Na+-translocating F1Fo-ATPase of Acetobacterium woodii: proposal for determinants of Na+ specificity as revealed by sequence comparisons. FEBS Lett. 404 (1997) 269-271. [PMID: 9119076]
Accepted name: arsenite-transporting ATPase
Reaction: ATP + H2O + arsenitein = ADP + phosphate + arseniteout
Systematic name: ATP phosphohydrolase (arsenite-exporting)
Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. A bacterial enzyme that usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. Exports arsenite and antimonite anions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Silver, S., Misra, T.K. and Laddaga, R.A. DNA sequence analysis of bacterial toxic heavy metal resistance. Biol. Trace Elem. Res. 21 (1989) 145-163. [PMID: 2484581]
2. Rosen, B.P., Weigel, U., Monticello, R.A. and Edwards, B.P. Molecular analysis of an anion pump: purification of the ArsC protein. Arch. Biochem. Biophys. 284 (1991) 381-385. [PMID: 1703401]
3. Bruhn, D.F., Li, J., Silver, S., Roberto, F. and Rosen, B.P. The arsenical resistance operon of IncN plasmid R46. FEMS Microbiol. Lett. 139 (1996) 149-153. [PMID: 8674982]
4. Zhou, T., Rosen, B.P. and Gatti, D.L. Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 921-924. [PMID: 10089335]
Accepted name: monosaccharide-transporting ATPase
Reaction: ATP + H2O + monosaccharideout = ADP + phosphate + monosaccharidein
Systematic name: ATP phosphohydrolase (monosaccharide-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [PMID: 1282354]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Kemner, J.M., Liang, S. and Nester, E.W. The Agrobacterium tumefaciens virulence gene chvE is part of a putative ABC-type sugar transport operon. J. Bacteriol. 179 (1997) 2452-2458. [PMID: 9079938]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Song, S. and Park, C. Utilization of D-ribose through D-xylose transporter. FEMS Microbiol. Lett. 163 (1998) 255-261. [PMID: 9673030]
6. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: oligosaccharide-transporting ATPase
Reaction: ATP + H2O + oligosaccharideout = ADP + phosphate + oligosaccharidein
Systematic name: ATP phosphohydrolase (disaccharide-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports lactose, melibiose and raffinose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [PMID: 1282354]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Tam, R. and Saier, M.H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57 (1993) 320-346. [PMID: 8336670]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Williams, S.G., Greenwood, J.A. and Jones, C.W. Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and β-galactosidase in Agrobacterium radiobacter. Mol. Microbiol. 6 (1992) 1755-1768. [PMID: 1630315]
Accepted name: maltose-transporting ATPase
Reaction: ATP + H2O + maltoseout = ADP + phosphate + maltosein
Systematic name: ATP phosphohydrolase (maltose-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import maltose and maltose oligosaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [PMID: 1282354]
2. Dassa, E. and Muir, S. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol. Microbiol. 7 (1993) 29-38. [PMID: 8437518]
3. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: glycerol-3-phosphate-transporting ATPase
Reaction: ATP + H2O + glycerol-3-phosphateout = ADP + phosphate + glycerol-3-phosphatein
Systematic name: ATP phosphohydrolase (glycerol-3-phosphate-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphorylated glycerol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
2. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
3. Bahl, H., Burchhardt, G. and Wienecke, A. Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes homologous to Escherichia coli genes encoding integral membrane components of binding-protein-dependent transport systems. FEMS Microbiol. Lett. 65 (1991) 83-87. [PMID: 1874408]
Accepted name: polar-amino-acid-transporting ATPase
Reaction: ATP + H2O + polar amino acidout = ADP + phosphate + polar amino acidin
Other name(s): histidine permease
Systematic name: ATP phosphohydrolase (polar-amino-acid-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Nikaido, K., Liu, P.Q. and Ferro-Luzzi Ames, G. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubilization, dimerization , and ATPase activity. J. Biol. Chem. 272 (1997) 27745-27752. [PMID: 9346917]
4. Walshaw, D.L., Lowthorpe, S., East, A. and Poole, P.S. Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity. FEBS Lett. 414 (1997) 397-401. [PMID: 9315727]
Accepted name: nonpolar-amino-acid-transporting ATPase
Reaction: ATP + H2O + nonpolar amino acidout = ADP + phosphate + nonpolar amino acidin
Systematic name: ATP phosphohydrolase (nonpolar-amino-acid-transporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import Leu, Ile and Val.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: oligopeptide-transporting ATPase
Reaction: ATP + H2O + oligopeptideout = ADP + phosphate + oligopeptidein
Other name(s): oligopeptide permease
Systematic name: ATP phosphohydrolase (oligopeptide-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports di- and oligopeptides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
4. Pearce, S.R., Mimmack, M.L., Gallagher, M.P., Gileadi, U., Hyde, S.C. and Higgins, C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 6 (1992) 47-57. [PMID: 1738314]
Accepted name: nickel-transporting ATPase
Reaction: ATP + H2O + Ni2+out = ADP + phosphate + Ni2+in
Systematic name: ATP phosphohydrolase (nickel-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Ni2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Hendricks, J.K. and Mobley, H.L. Helicobacter pylori ABC transporter: effect of allelic exchange mutagenesis on urease activity. J. Bacteriol. 179 (1997) 5892-5902. [PMID: 9294450]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: sulfate-transporting ATPase
Reaction: ATP + H2O + sulfateout = ADP + phosphate + sulfatein
Systematic name: ATP phosphohydrolase (sulfate-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports sulfate and thiosulfate anions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sirko, A., Zatyka, M., Sadowy, E. and Hulanicka, D. Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins. J. Bacteriol. 177 (1995) 4134-4136. [PMID: 7608089]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: nitrate-transporting ATPase
Reaction: ATP + H2O + nitrateout = ADP + phosphate + nitratein
Systematic name: ATP phosphohydrolase (nitrate-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports NO3-, NO2- and OCN-.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Omata, T. Structure, function and regulation of the nitrate transport system of the cyanobacterium Synechococcus sp. PCC7942. Plant Cell Physiol. 36 (1995) 207-213.
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: phosphate-transporting ATPase
Reaction: ATP + H2O + phosphateout = ADP + phosphate + phosphatein
Other name(s): ABC phosphate transporter
Systematic name: ATP phosphohydrolase (phosphate-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphate anions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Webb, D.C., Rosenberg, H. and Cox, G.B. Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. A role for proline residues in transmembrane helices. J. Biol. Chem. 267 (1992) 24661-24668. [PMID: 1447208]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Braibant, M., LeFevre, P., de Wit, L., Ooms, J., Peirs, P., Huygen, K., Wattiez, R. and Content, J. Identification of a second Mycobacterium tuberculosis gene cluster encoding proteins of an ABC phosphate transporter. FEBS Lett. 394 (1996) 206-212. [PMID: 8843165]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: phosphonate-transporting ATPase
Reaction: ATP + H2O + phosphonateout = ADP + phosphate + phosphonatein
Systematic name: ATP phosphohydrolase (phosphonate-transporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphonate and organophosphate anions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wanner, B.L. and Metcalf, W.W. Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation. FEMS Microbiol. Lett. 79 (1992) 133-139. [PMID: 1335942]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: molybdate-transporting ATPase
Reaction: ATP + H2O + molybdateout = ADP + phosphate + molybdatein
Systematic name: ATP phosphohydrolase (molybdate-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports molybdate anions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Grunden, A.M. and Shanmugam, K.T. Molybdate transport and regulation in bacteria. Arch. Mikrobiol. 168 (1997) 345-354. [PMID: 9325422]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: Fe3+-transporting ATPase
Reaction: ATP + H2O + Fe3+out = ADP + phosphate + Fe3+in
Systematic name: ATP phosphohydrolase (ferric-ion-transporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports ferric cations.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Angerer, A., Klupp, B. and Braun, V. Iron transport systems of Serratia marcescens. J. Bacteriol. 174 (1992) 1378-1387. [PMID: 1531225]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Khun, H.H., Kirby, S.D. and Lee, B.C. A Neisseria meningitidis fbp ABC mutant is incapable of using nonheme iron for growth. Infect. Immun. 66 (1998) 2330-2336. [PMID: 9573125]
Accepted name: polyamine-transporting ATPase
Reaction: ATP + H2O + polyamineout = ADP + phosphate + polyaminein
Systematic name: ATP phosphohydrolase (polyamine-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kashiwagi, K., Miyamoto, S., Nukui, E., Kobayashi, H. and Igarashi, K. Functions of potA and potD proteins in spermidine - preferential uptake system in Escherichia coli. J. Biol. Chem. 268 (1993) 19358-19363. [PMID: 8366082]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: quaternary-amine-transporting ATPase
Reaction: ATP + H2O + quaternary amineout = ADP + phosphate + quaternary aminein
Systematic name: ATP phosphohydrolase (quaternary-amine-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports betaine and glycine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Kempf, B., Gade, J. and Bremer, E. Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant. J. Bacteriol. 179 (1997) 6213-6220. [PMID: 9335265]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: vitamin B12-transporting ATPase
Reaction: ATP + H2O + vitamin B12out = ADP + phosphate + vitamin B12in
Systematic name: ATP phosphohydrolase (vitamin B12-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports cobalamin derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Friedrich, M.J., de Veaux, L.C. and Kadner, R.J. Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems. J. Bacteriol. 167 (1986) 928-934. [PMID: 3528129]
Accepted name: iron-chelate-transporting ATPase
Reaction: ATP + H2O + iron chelateout = ADP + phosphate + iron chelatein
Systematic name: ATP phosphohydrolase (iron-chelate-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Fe-enterobactin, Fe-dicitrate, Fe-hydroxamate and other siderophores.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shea, C.M. and McIntosh, M.A. Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding-protein-dependent systems in Escherichia coli. Mol. Microbiol. 5 (1991) 1415-1428. [PMID: 1838574]
2. Koster, W. and Böhm, B. Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport. Mol. Gen. Genet. 232 (1992) 399-407. [PMID: 1588908]
3. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Mademidis, A. and Koster, W. Transport activity of FhuA, FhuC, FhuD and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake. Mol. Gen. Genet. 258 (1998) 156-165. [PMID: 9613584]
Accepted name: manganese-transporting ATPase
Reaction: ATP + H2O + Mn2+out = ADP + phosphate + Mn2+in
Other name(s): ABC-type manganese permease complex
Systematic name: ATP phosphohydrolase (manganese-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Mn2+, Zn2+ and iron chelates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Novak, R., Braun, J.S., Charpentier, E. and Tuomanen, E. Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa. Mol. Microbiol. 29 (1998) 1285-1296. [PMID: 9767595]
4. Kolenbrander, P.E., Andersen, R.N., Baker, R.A. and Jenkinson, H.F. The adhesion-assoiated aca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn2+ uptake. J. Bacteriol. 180 (1998) 290-295. [PMID: 9440518]
Accepted name: taurine-transporting ATPase
Reaction: ATP + H2O + taurineout = ADP + phosphate + taurinein
Systematic name: ATP phosphohydrolase (taurine-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports taurine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. van der Ploeg, J.R., Weiss, M.A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M.A. and Leisinger, T. Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178 (1996) 5438-5446. [PMID: 8808933]
Accepted name: guanine-transporting ATPase
Reaction: ATP + H2O + guanineout = ADP + phosphate + guaninein
Systematic name: ATP phosphohydrolase (guanine-importing)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A eukaryotic enzyme that imports guanine and tryptophan (it contains a single ATP-binding site).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Dreesen, T.D., Johnson, D.H and Henikoff, S. The brown protein of Drosophila melanogaster is similar to the white protein and to components of active transport complexes. Mol. Cell Biol. 8 (1988) 5206-5215. [PMID: 3149712]
2. Tearle, R.G., Belote, J.M., McKeown, M., Baker, B.S. and Howells, A.J. Cloning and characterization of the scarlet gene of Drosophila melanogaster. Genetics 122 (1989) 595-606. [PMID: 89339145]
3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: capsular-polysaccharide-transporting ATPase
Reaction: ATP + H2O + capsular polysaccharidein = ADP + phosphate + capsular polysaccharideout
Systematic name: ATP phosphohydrolase (capsular-polysaccharide-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme that exports capsular polysaccharide from Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [PMID: 8302219]
2. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [PMID: 9274022]
3. Pigeon, R.P. and Silver, R.P. Analysis of the G93E mutant allele of KpsM, the membrane component of an ABC transporter involved in polysialic acid translocation in Escherichia coli K1.FEMS. Microbiol. Lett. 156 (1997) 217-222. [PMID: 9513268]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: lipopolysaccharide-transporting ATPase
Reaction: ATP + H2O + lipopolysaccharidein = ADP + phosphate + lipopolysaccharideout
Systematic name: ATP phosphohydrolase (lipopolysaccharide-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Enzymes of Gram-negative bacteria that export lipo-oligosaccharides and lipopolysaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [PMID: 8302219]
2. Fernandez-Lopez, M., D'Haeze, W., Mergaert, P., Verplancke, C., Prome, J.C., Van Montagu, M. and Holstens, M. Role of nod1and nodJ in lipo-chitooligosaccharide secretion in Azorhizobium caulinodans and Escherichia coli. Mol. Microbiol. 20 (1996) 993-1000. [PMID: 8809752]
3. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [PMID: 9274022]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: teichoic-acid-transporting ATPase
Reaction: ATP + H2O + teichoic acidin = ADP + phosphate + teichoic acidout
Systematic name: ATP phosphohydrolase (teichoic-acid-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-positive bacteria that exports teichoic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [PMID: 8302219]
2. Lazarevic, V. and Karamoto, D. The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids. Mol. Microbiol. 16 (1995) 345-355. [PMID: 7565096]
3. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [PMID: 9274022]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: heme-transporting ATPase
Reaction: ATP + H2O + hemein = ADP + phosphate + hemeout
Systematic name: ATP phosphohydrolase (heme-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-negative bacteria that exports heme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
2. Jekabsons, W. and Schuster, W. orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria. Mol. Gen. Genet. 246 (1995) 166-173. [PMID: 7862087]
3. Ramseier, T.M., Winteler, H.V. and Hennecke, H. Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes. J. Biol. Chem. 266 (1991) 7793-7803. [PMID: 1850420]
Accepted name: β-glucan-transporting ATPase
Reaction: ATP + H2O + β-glucanin = ADP + phosphate + β-glucanout
Systematic name: ATP phosphohydrolase (β-glucan-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-negative bacteria that exports β-glucan.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [PMID: 8302219]
2. Becker, A., Kuster, H., Niehaus, K. and Puhler, A. Extension of the Rhizobium meliloti succinoglycan biosynthesis gene cluster: identification of the exsA gene encoding an ABC transporter protein, and the exsB gene which probably codes for a regulator of succinoglycan biosynthesis. Mol. Gen. Genet. 249 (1995) 487-497. [PMID: 8544814]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: peptide-transporting ATPase
Reaction: ATP + H2O + peptidein = ADP + phosphate + peptideout
Systematic name: ATP phosphohydrolase (peptide-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A family of enzymes that exports α-hemolysin, cyclolysin, colicin V and siderophores from Gram-negative bacteria, and bacteriocin, subtilin, competence factor and pediocin from Gram-positive bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Klein, C. and Entian, K.D. Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633. Appl. Environ. Microbiol. 60 (1994) 2793-2801. [PMID: 8085823]
2. Momburg, F., Roelse, J., Howard, J.C., Butcher, G.W., Hammerling, G.J. and Neefjes, J.J. Selectivity of MHC-encoded peptide transporters from human, mouse and rat. Nature 367 (1994) 648-651. [PMID: 8107849]
3. Binet, R., Létoffé, S., Ghigo, J.M., Delepaire, P. and Wanderman, C. Protein secretion by Gram-negative bacterial ABC exporters - a review. Gene 192 (1997) 7-11. [PMID: 9224868]
Accepted name: xenobiotic-transporting ATPase
Reaction: ATP + H2O + xenobioticin = ADP + phosphate + xenobioticout
Other name(s): multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting)
Systematic name: ATP phosphohydrolase (xenobiotic-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. The enzyme from Gram-positive bacteria and eukaryotic cells export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them transport glutathione—drug conjugates. Some also show some 'flippase' (phospholipid-translocating ATPase; EC 3.6.3.1) activity.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Bellamy, W.T. P-glycoproteins and multidrug resistance. Annu. Rev. Pharmac. Toxicol. 36 (1996) 161-183. [PMID: 8725386]
2. Frijters, C.M., Ottenhoff, R., Van Wijland, M.J., Van Nieuwkerk, C., Groen, A.K. and Oude-Elferink, R.P. Influence of bile salts on hepatic mdr2 P-glycoprotein expression. Adv. Enzyme Regul. 36 (1996) 351-363. [PMID: 8869755]
3. Keppler, D., König, J. and Buchler, M. The canalicular multidrug resistance protein, cMRP/MRP2, a novel conjugate export pump expressed in the apical membrane of hepatocytes. Adv. Enzyme Regul. 37 (1997) 321-333. [PMID: 9381978]
4. Loe, D.W., Deeley, R.G. and Cole, S.P. Characterization of vincristine transport by the Mr 190,000 multidrug resistance protein (MRP): evidence for cotransport with reduced glutathione. Cancer Res. 58 (1998) 5130-5136. [PMID: 9823323]
5. van Veen, H.W. and Konings, W.N. The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta 1365 (1998) 31-36. [PMID: 9693718]
6. Griffiths, J.K. and Sansom, C.E. (Ed.), The Transporter Factsbook, Academic Press, San Diego, 1998,
7. Prasad, R., De Wergifosse, P., Goffeau, A. and Balzi, E. Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals. Curr. Genet. 27 (1995) 320-329. [PMID: 7614555]
8. Nagao, K., Taguchi, Y., Arioka, M., Kadokura, H., Takatsuki, A., Yoda, K. and Yamasaki, M. bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily. J. Bacteriol. 177 (1995) 1536-1543. [PMID: 7883711]
9. Mahé, Y., Lemoine, Y. and Kuchler, K. The ATP-binding cassette transporters Pdr5 and Snq2 of Saccharomyces cerevisiae can mediate transport of steroids in vivo. J. Biol. Chem. 271 (1996) 25167-25172. [PMID: 8810273]
[EC 3.6.3.45 Deleted entry: steroid-transporting ATPase. Now included with EC 3.6.3.44, xenobiotic-transporting ATPase (EC 3.6.3.45 created 2000, deleted 2006)]
Accepted name: cadmium-transporting ATPase
Reaction: ATP + H2O = ADP + phosphate
Other name: yeast cadmium factor
Systematic name: ATP phosphohydrolase (heavy-metal-exporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509-6517. [PMID: 8626454]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: fatty-acyl-CoA-transporting ATPase
Reaction: ATP + H2O + fatty acyl CoAcis = ADP + phosphate + fatty acyl CoAtrans
Systematic name: ATP phosphohydrolase (fatty-acyl-CoA-transporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kamijo, K., Taketani, S., Yokota, S., Osumi, T. and Hashimoto, T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glcoprotein)-related ATP-binding protein superfamily. J. Biol. Chem. 265 (1990) 4534-4540. [PMID: 1968461]
2. Hettema, E.H., van Roermund, C.W.T., Distel, B., van den Berg. M., Vilela, C., Rodrigues-Posada, C., Wanders, R.J.A. and Tabak, H.F. The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. EMBO J. 15 (1996) 3813-3822. [PMID: 8670886]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: α-factor-transporting ATPase
Reaction: ATP + H2O + α-factorin = ADP + phosphate + α-factorout
Systematic name: ATP phosphohydrolase (α-factor-transporting)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports the α-factor sex pheromone.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Michaelis, S. STE6, the yeast α-factor exporter. Semin. Cell Biol. 4 (1993) 17-27. [PMID: 8095825]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: channel-conductance-controlling ATPase
Reaction: ATP + H2O = ADP + phosphate
Other name: cystic-fibrosis membrane-conductance-regulating protein
Systematic name: ATP phosphohydrolase (channel-conductance-controlling)
Comments: ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An animal enzyme that is active in forming a chloride channel, the absence of which brings about cystic fibrosis. It is also involved in the functioning of other transmembrane channels.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Chen, M. and Zhang, J.T. Membrane insertion, processing, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes. Mol. Membr. Biol. 13 (1996) 33-40. [PMID: 9147660]
2. Tusnady, G.E., Bakos, E., Varadi, A. and Sarkadi, B. Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters. FEBS Lett. 402 (1997) 1-3. [PMID: 9013845]
3. Sheppard, D.N. and Welsh, M.J. Structure and function of the CFTR chloride channel. Physiol. Rev. 79 (1999) S23-S45. [PMID: 9922375]
Accepted name: protein-secreting ATPase
Reaction: ATP + H2O = ADP + phosphate
Systematic name: ATP phosphohydrolase (protein-secreting)
Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. There are several families of enzymes included here, e.g. ATP-hydrolysing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Saier, M.H., Jr., Tam. R., Reizer, A. and Reizer, J. Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol. Microbiol. 11 (1994) 841-847. [PMID: 8022262]
2. Mecsas, J. and Strauss, E.J. Molecular mechanisms of bacterial virulence: type III secretion and pathogenicity islands. Emerg. Infect. Diseases. 2 (1996) 270-288. [PMID: 8969244]
3. Thomas, J.D., Reeves, P.J. and Salmond, G.P. The general secretion pathway of Erwinia carotovora subsp. carotovora: analysis of the membrane topology of OutC and OutF. Microbiology 143 (1997) 713-720. [PMID: 9084158]
4. Baker, B., Zambryski, P., Staskawicz, B. and Dinesh-Kumar, S.P. Signaling in plant-microbe interactions. Science 276 (1997) 726-733. [PMID: 9115193]
5. Martinez, A., Ostrovsky, P. and Nunn, D.N. Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion. Mol. Microbiol. 28 (1998) 1235-1246. [PMID: 9680212]
6. Schuch, R. and Maurelli, A.T. The mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasin translocation. Infect. Immun. 67 (1999) 1982-1991. [PMID: 10085046]
Accepted name: mitochondrial protein-transporting ATPase
Reaction: ATP + H2O = ADP + phosphate
Systematic name: ATP phosphohydrolase (mitochondrial protein-importing)
Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex. (TIM is the protein transport machinery of the inner mitochondrial membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bomer, U., Meijer, M., Maarse, A.C., Honlinger, A., Dekker, P.J., Pfanner, N. and Rassow, J. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane. EMBO J. 16 (1997) 2205-2216. [PMID: 9171336]
2. Berthold, J., Bauer, M.F., Schneider, H.C., Klaus, C., Dietmeier, K., Neupert, W. and Brunner, M. The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP-driving system. Cell 81 (1995) 1085-1093. [PMID: 7600576]
3. Voos, W., Martin, H., Krimmer, T. and Pfanner, N. Mechanisms of protein translocation into mitochondria. Biochim. Biophys. Acta 1422 (1999) 235-254. [PMID: 10548718]
Accepted name: chloroplast protein-transporting ATPase
Reaction: ATP + H2O = ADP + phosphate
Systematic name: ATP phosphohydrolase (chloroplast protein-importing)
Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Cline, K., Ettinger, N.F. and Theg, S.M. Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J. Biol. Chem. 267 (1992) 2688-2696. [PMID: 1733965]
2. Nakai, M., Goto, A., Nohara, T., Sugito, D. and Endo, T. Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J. Biol. Chem. 269 (1994) 31338-33341. [PMID: 7989297]
3. Scott, S.V. and Theg, S.M. A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implications. J. Cell Biol. 132 (1996) 63-75. [PMID: 8567731]
Accepted name: Ag+-exporting ATPase
Reaction: ATP + H2O + Ag+in = ADP + phosphate + Ag+out
Systematic name: ATP phosphohydrolase (Ag+-exporting)
Comments: A P-type ATPase that exports Ag+ ions from pathogenic microorganisms as well as from some animal tissues.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gupta, A., Matsui, K., Lo, J.F. and Silver, S. Molecular basis for resistance to silver cations in Salmonella. Nature Med. 5 (1999) 183-188. [PMID: 9930866]
2. Bury, N.R., Grosell, M., Grover, A.K. and Wood, C.M. ATP-dependent silver transport across the basolateral membrane of rainbow trout gills. Toxicol. Appl. Pharmacol. 159 (1999) 1-8. [PMID: 10448119]